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Papers In Press, published online ahead of print July 24, 2002
Department of Medicine, Northwestern University, Chicago, IL 60611
Corresponding Author: v-cryns{at}northwestern.edu
Myoblasts respond to growth factor deprivation either by differentiating into multinucleated myotubes or by undergoing apoptosis; hence, the acquisition of apoptosis-resistance by myogenic precursors is essential for their development. Here, we demonstrate that the expression of the small heat shock protein
J. Biol. Chem, 10.1074/jbc.M201770200
Submitted on February 21, 2002
Revised on July 24, 2002
Accepted on July 24, 2002
The small heat shock protein
B-crystallin negatively regulates apoptosis during myogenic differentiation by inhibiting caspase-3 Activation
B-crystallin is selectively induced in C2C12 myoblasts that are resistant to differentiation-induced apoptosis, and we show that this induction occurs at an early stage in their differentiation in vitro. In contrast, the expression of several known anti-apoptotic proteins (FLIP, XIAP, Bcl-xL) was not altered during myogenesis. We also demonstrate that ectopic expression of B-crystallin, but not the closely related small heat shock protein Hsp27, renders C2C12 myoblasts resistant to differentiation-induced apoptosis. Furthermore, we show that the myopathy-causing R120G B-crystallin mutant is partly impaired in its cytoprotective function, while a pseudophosphorylation B-crystallin mutant that mimics stress-induced phosphorylation is completely devoid of anti-apoptotic activity. Finally, we demonstrate that B-crystallin negatively regulates apoptosis during myogenesis by inhibiting the proteolytic activation of caspase-3, while the R120G and pseudophosphorylation mutants are defective in this function. Taken together, our findings indicate that B-crystallin is a novel negative regulator of myogenic apoptosis that directly links the differentiation program to apoptosis-resistance.
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